Title : Identification of an alternatively spliced seprase mRNA that encodes a novel intracellular isoform - Goldstein_2000_J.Biol.Chem_275_2554 |
Author(s) : Goldstein LA , Chen WT |
Ref : Journal of Biological Chemistry , 275 :2554 , 2000 |
Abstract :
Seprase is a homodimeric 170-kDa integral membrane gelatinase that is related to the ectoenzyme dipeptidyl peptidase IV. We have identified an alternatively spliced seprase messenger from the human melanoma cell line LOX that encodes a novel truncated isoform, seprase-s. The splice variant mRNA is generated by an out-of-frame deletion of a 1223-base pair exonic region that encodes part of the cytoplasmic tail, transmembrane, and the membrane proximal-central regions of the extracellular domain (Val(5) through Ser(412)) of the seprase 97-kDa subunit (seprase-l). The seprase-s mRNA has an elongated 5' leader (548 nucleotides) that harbors at least two upstream open reading frames that inhibit seprase-s expression from a downstream major open reading frame. Deletion mutagenesis of the wild type splice variant cDNA confirms that initiation of the seprase-s coding sequence begins with an ATG codon that corresponds to Met(522) of seprase-l. The seprase-s open reading frame encodes a 239-amino acid polypeptide with an M(r) approximately 27,000 that precisely overlaps the carboxyl-terminal catalytic region of seprase-l. |
PubMedSearch : Goldstein_2000_J.Biol.Chem_275_2554 |
PubMedID: 10644713 |
Gene_locus related to this paper: human-FAP |
Gene_locus | human-FAP |
Goldstein LA, Chen WT (2000)
Identification of an alternatively spliced seprase mRNA that encodes a novel intracellular isoform
Journal of Biological Chemistry
275 :2554
Goldstein LA, Chen WT (2000)
Journal of Biological Chemistry
275 :2554